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PMID: 8018721 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.

Biochimica et biophysica acta ·Vol. 1218 ·No. 2 ·1994-06-21 ·Pages 199-201

Walsh TR, Hall L, Assinder SJ, Nichols WW, Cartwright SJ, MacGowan AP, Bennett PM

Abstract

The amino acid sequence deduced from the L1 beta-lactamase gene of Xanthomonas maltophilia shows a significant variation from that of the CphA and Blm metallo-beta-lactamases of Aeromonas hydrophila and Bacillus cereus, respectively. Whilst the N-terminus of the L1 protein shows some similarity, particularly at the histidine residues previously suggested as a zinc-binding motif, the C-terminus of the protein demonstrates very little similarity. Such differences amongst this group of enzymes would argue for at least three subclasses within the Group 3 beta-lactamases. However, in order to predict their phylogenetic ancestry more sequence data are required from other possible metallo-beta-lactamases.

MeSH Terms
Amino Acid Sequence Base Sequence Molecular Sequence Data Sequence Alignment Xanthomonas/genetics beta-Lactamases/genetics
Chemicals
beta-lactamase L1 beta-Lactamases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Walsh T R
Department of Microbiology and Pathology, University of Bristol, UK.
Hall L
Assinder S J
Nichols W W
Cartwright S J
MacGowan A P
Bennett P M
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1994-06-21
Pages
199-201
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Databases
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